Document 13055427

FtsZ proteins in Physcomitrella: more than just chloroplast division
Anja Martin*; Louis Gremillon; Gabriele Schween; Ralf Reski; Eric Sarnighausen
Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1,
79104 Freiburg, Germany
*e-mail: [email protected], phone: +49 761 203-6940
Plastids as well as bacteria divide by binary fission. In bacteria, the division process is
mediated by the action of the FtsZ (filamentous temperature sensitive Z) protein which
forms a contractile ring at the future division site.
Plants have acquired plastids through an endosymbiotic event. An ftsZ gene from an
engulfed cyanobacterium was transferred to the host nucleus, was duplicated and
equipped with sequences coding for chloroplast-targeting signals. In plants, FtsZ
proteins group into two families (FtsZ1 and 2) and function in plastid division.
In order to analyze the subcellular localization of FtsZ proteins in Physcomitrella patens
we employed ftsZ:gfp fusions which revealed plastidic localization for FtsZ 1-1, 2-1, and
2-2 whereas FtsZ1-2 undergoes dual targeting and is found in plastids and the cytosol [1,
2]. As shown previously, the targeted knockout of ftsZ2-1 gave rise to plants with
macrochloroplasts underlining the protein’s involvement in organelle division [3].
To further elucidate the individual functions of FtsZ proteins in Physcomitrella
knockouts of ftsZ1-1, 1-2, and 2-2 were generated. Compared to wild type, knockout
plants of ftsZ1-1 and 2-2 reveal only mild phenotypic aberrations. In contrast, loss of
ftsZ1-2 leads to severe alterations in plant morphology and development. Compared to
wild type, ΔftsZ1-2 lines grow slower and exhibit shorter gametophores. Chloroplast
shape and size in leaflet, chloronema and caulonema cells are highly irregular.
Protonema cell dimensions and leaflet cell patterning are altered as well. We therefore
conclude that in Physcomitrella FtsZ1-2 is involved not only in plastid division but also
plays an important role in shaping cells and chloroplasts.
Financial support by Deutsche Forschungsgemeinschaft (SFB 388) is gratefully
[1] Kiessling, J., Kruse, S., Rensing, S.A., Harter, K., Decker, E.L., Reski, R. (2000)
J Cell Biol. 151: 945-950
[2] Kiessling, J., Martin A., Gremillon, L., Rensing, S.A., Nick, P., Sarnighausen, E.,
Reski, R. (2004) EMBO R. 5: 889-894
[3] Strepp, R., Scholz, S., Kruse, S., Speth, V., Reski, R. (1998) PNAS 95 : 43684373